Ablation of myosin-binding protein-C accelerates force development in mouse myocardium - Wikidata - awgldk - TriplyDB

Ablation of myosin-binding protein-C accelerates force development in mouse myocardium

Ablation of myosin-binding protein-C accelerates force development in mouse myocardium

http://www.wikidata.org/entity/Q28300076

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Support for a trimeric collar of myosin binding protein C in cardiac and fast skeletal muscle, but not in slow skeletal muscle Neonatal mouse-derived engineered cardiac tissue: a novel model system for studying genetic heart disease Contractile apparatus dysfunction early in the pathophysiology of diabetic cardiomyopathy The myosin-binding protein C motif binds to F-actin in a phosphorylation-sensitive manner In vivo left ventricular functional capacity is compromised in cMyBP-C null mice Radial displacement of myosin cross-bridges in mouse myocardium due to ablation of myosin binding protein-C In the thick of it: HCM-causing mutations in myosin binding proteins of the thick filament The structure of isolated cardiac Myosin thick filaments from cardiac Myosin binding protein-C knockout mice.Cardiac myosin binding protein C and MAP-kinase activating death domain-containing gene polymorphisms and diastolic heart failure.Zebrafish cardiac muscle thick filaments: isolation technique and three-dimensional structure.Protein kinase A-mediated phosphorylation of cMyBP-C increases proximity of myosin heads to actin in resting myocardium.Phosphorylation of cMyBP-C affects contractile mechanisms in a site-specific manner Cardiac troponin T, a sarcomeric AKAP, tethers protein kinase A at the myofilaments.Increased Postnatal Cardiac Hyperplasia Precedes Cardiomyocyte Hypertrophy in a Model of Hypertrophic Cardiomyopathy.Normal passive viscoelasticity but abnormal myofibrillar force generation in human hypertrophic cardiomyopathy.Altered in vivo left ventricular torsion and principal strains in hypothyroid rats Protein kinase A-induced myofilament desensitization to Ca(2+) as a result of phosphorylation of cardiac myosin-binding protein C Identification of novel protein kinase A phosphorylation sites in the M-domain of human and murine cardiac myosin binding protein-C using mass spectrometry analysis.Length-dependent changes in contractile dynamics are blunted due to cardiac myosin binding protein-C ablation.Kinetics of cardiac myosin isoforms in mouse myocardium are affected differently by presence of myosin binding protein-C Roles for cardiac MyBP-C in maintaining myofilament lattice rigidity and prolonging myosin cross-bridge lifetime.Cardiac myosin binding protein C insufficiency leads to early onset of mechanical dysfunction.Cardiac myosin binding protein-C: redefining its structure and function.Altered contractility of skeletal muscle in mice deficient in titin's M-band region.Molecular effects of the myosin activator omecamtiv mecarbil on contractile properties of skinned myocardium lacking cardiac myosin binding protein-C ADP-stimulated contraction: A predictor of thin-filament activation in cardiac disease.Cardiac myosin binding protein-C restricts intrafilament torsional dynamics of actin in a phosphorylation-dependent manner.Ablation of cardiac myosin-binding protein-C accelerates contractile kinetics in engineered cardiac tissue.Cardiac Myosin Binding Protein-C Phosphorylation Modulates Myofilament Length-Dependent Activation Cardiac Myosin-binding protein C modulates the tuning of the molecular motor in the heart Slowing of contractile kinetics by myosin-binding protein C can be explained by its cooperative binding to the thin filament.S-glutathiolation impairs phosphoregulation and function of cardiac myosin-binding protein C in human heart failure.In vivo cardiac myosin binding protein C gene transfer rescues myofilament contractile dysfunction in cardiac myosin binding protein C null mice Ablation of cardiac myosin binding protein-C disrupts the super-relaxed state of myosin in murine cardiomyocytes.Contribution of the myosin binding protein C motif to functional effects in permeabilized rat trabeculae Characterization of the cardiac myosin binding protein-C phosphoproteome in healthy and failing human hearts Impaired contractile function due to decreased cardiac myosin binding protein C content in the sarcomere Ionic bases for electrical remodeling of the canine cardiac ventricle.Cardiac myosin binding protein-C is essential for thick-filament stability and flexural rigidity Expression patterns of cardiac myofilament proteins: genomic and protein analysis of surgical myectomy tissue from patients with obstructive hypertrophic cardiomyopathy.

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P2860

Ablation of myosin-binding protein-C accelerates force development in mouse myocardium

http://www.wikidata.org/entity/Q28300076

description

2006 nî lūn-bûn

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2006 թուականի Յունիսին հրատարակուած գիտական յօդուած

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2006 թվականի հունիսին հրատարակված գիտական հոդված

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2006年の論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年论文

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name

Ablation of myosin-binding protein-C accelerates force development in mouse myocardium

@ast

Ablation of myosin-binding protein-C accelerates force development in mouse myocardium

@en

Ablation of myosin-binding protein-C accelerates force development in mouse myocardium

@nl

type

label

Ablation of myosin-binding protein-C accelerates force development in mouse myocardium

@ast

Ablation of myosin-binding protein-C accelerates force development in mouse myocardium

@en

Ablation of myosin-binding protein-C accelerates force development in mouse myocardium

@nl

prefLabel

Ablation of myosin-binding protein-C accelerates force development in mouse myocardium

@ast

Ablation of myosin-binding protein-C accelerates force development in mouse myocardium

@en

Ablation of myosin-binding protein-C accelerates force development in mouse myocardium

@nl

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BIOPHYSJ.105.078147

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Biophysical Journal

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Ablation of myosin-binding protein-C accelerates force development in mouse myocardium

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P2093

Daniel P Fitzsimons

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Julian E Stelzer

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Richard L Moss

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P2860

Mutations in beta-myosin S2 that cause familial hypertrophic cardiomyopathy (FHC) abolish the interaction with the regulatory domain of myosin-binding protein-C

Cardiac myosin binding protein C: its role in physiology and disease

The interaction of C-protein with heavy meromyosin and subfragment-2

Myosin binding protein C, a phosphorylation-dependent force regulator in muscle that controls the attachment of myosin heads by its interaction with myosin S2

Loaded shortening, power output, and rate of force redevelopment are increased with knockout of cardiac myosin binding protein-C

Hypertrophic cardiomyopathy in cardiac myosin binding protein-C knockout mice

A new protein of the thick filaments of vertebrate skeletal myofibrils. Extractions, purification and characterization

Basal myosin light chain phosphorylation is a determinant of Ca2+ sensitivity of force and activation dependence of the kinetics of myocardial force development

A fluorescent probe study of Ca2+ binding to the Ca2+-specific sites of cardiac troponin and troponin C

Binding of myosin binding protein-C to myosin subfragment S2 affects contractility independent of a tether mechanism

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